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Myosin VI motor domain in the pre-transition state

Analyse Myosin VI motor domain in the pre-transition state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5O2L
Type: protein
Length: 763 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Unconventional myosin-VI
UniProt: F1RQI7
Ligands: ADP, BEF, MG
Pockets: 6 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Unconventional myosin-VI	protein	763	48% helix, 17% strand	F1RQI7

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
BEF · Beryllium trifluoride ion · ligand · chains A
MG · Magnesium ion · metal · chains A
GOL · Glycerol · additive · 8 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1129	0.82	0.84	127	ADP, MG, BEF
2	63	0.72	0.97	19	GOL
3	388	0.61	0.76	43	empty
4	127	0.49	0.79	18	empty
5	84	0.36	0.76	17	empty

Compared structures

5O2L · Myosin VI motor domain in the Pre-Transition State · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt F1RQI7
Elsewhere: RCSB PDB 5O2L · PDBe 5O2L · UniProt F1RQI7

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